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SCP22_ARATH
ID   SCP22_ARATH             Reviewed;         464 AA.
AC   Q1PF08; O82228; Q1PF09;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Serine carboxypeptidase-like 22;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL22; OrderedLocusNames=At2g24000; ORFNames=T29E15.20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
RP   GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX   PubMed=15908604; DOI=10.1104/pp.104.057950;
RA   Fraser C.M., Rider L.W., Chapple C.;
RT   "An expression and bioinformatics analysis of the Arabidopsis serine
RT   carboxypeptidase-like gene family.";
RL   Plant Physiol. 138:1136-1148(2005).
CC   -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q1PF08-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q1PF08-2; Sequence=VSP_022849;
CC   -!- TISSUE SPECIFICITY: Expression not detected.
CC       {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC63668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC005170; AAC63668.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07515.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07516.1; -; Genomic_DNA.
DR   EMBL; DQ446557; ABE65855.1; -; mRNA.
DR   EMBL; DQ446558; ABE65856.1; -; mRNA.
DR   PIR; D84631; D84631.
DR   RefSeq; NP_001077950.1; NM_001084481.1. [Q1PF08-2]
DR   RefSeq; NP_179978.2; NM_127962.3. [Q1PF08-1]
DR   AlphaFoldDB; Q1PF08; -.
DR   SMR; Q1PF08; -.
DR   STRING; 3702.AT2G24000.1; -.
DR   ESTHER; arath-SCP22; Carboxypeptidase_S10.
DR   MEROPS; S10.A35; -.
DR   PaxDb; Q1PF08; -.
DR   PRIDE; Q1PF08; -.
DR   ProteomicsDB; 226629; -. [Q1PF08-1]
DR   EnsemblPlants; AT2G24000.1; AT2G24000.1; AT2G24000. [Q1PF08-1]
DR   EnsemblPlants; AT2G24000.2; AT2G24000.2; AT2G24000. [Q1PF08-2]
DR   GeneID; 816934; -.
DR   Gramene; AT2G24000.1; AT2G24000.1; AT2G24000. [Q1PF08-1]
DR   Gramene; AT2G24000.2; AT2G24000.2; AT2G24000. [Q1PF08-2]
DR   KEGG; ath:AT2G24000; -.
DR   Araport; AT2G24000; -.
DR   TAIR; locus:2061436; AT2G24000.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_0_1; -.
DR   InParanoid; Q1PF08; -.
DR   OMA; NFSWNTE; -.
DR   PhylomeDB; Q1PF08; -.
DR   PRO; PR:Q1PF08; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q1PF08; baseline and differential.
DR   Genevisible; Q1PF08; AT.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Carboxypeptidase; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..464
FT                   /note="Serine carboxypeptidase-like 22"
FT                   /id="PRO_0000274638"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        437
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        86..346
FT                   /evidence="ECO:0000250"
FT   DISULFID        247..258
FT                   /evidence="ECO:0000250"
FT   DISULFID        282..314
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         119..181
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17147637"
FT                   /id="VSP_022849"
SQ   SEQUENCE   464 AA;  53106 MW;  DFACB79F8A5BE6E4 CRC64;
     MARTHLLFLL FVLLSLATSS TSTKEQEEDR IKALPGQPKV GFSQFSGYVT VNESHGRSLF
     YWLTESSSHS PHTKPLLLWL NGGPGCSSIA YGASEEIGPF RISKTGCNLY LNNFSWNTEA
     NLLFLESPVG VGFSYTNTSS DFEESGDERT AQENLIFLIS WMSRFPQYRY RDFYIVGESY
     AGHYVPQLAQ KIHEYNNAYK NPVINLKGFM VGNPEMDKNN DRLGTITYWW SHAMISDASY
     NRILKNCDFT ADRFSKECDS AIYVAAADFG DIDQYSIYTP KCVPPQDQTN QTKFEQMMQM
     HTTKRFLEDQ YDPCTENYAE IYYNRPEVQR AMHANHTAIP YKWTACSDSV FNNWNWRDSD
     NSMLPIYKEL IAAGLRIWVY SGDTDSVIPV TATRYSLGKL NLRVKTRWYP WYSGNQVGGR
     TEVYEGLTFV TVRGAGHEVP FFQPQSALIL LRSFLAGNEL SRSY
 
 
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